1VYI
Structure of the c-terminal domain of the polymerase cofactor of rabies virus: insights in function and evolution.
Summary for 1VYI
| Entry DOI | 10.2210/pdb1vyi/pdb |
| Descriptor | RNA POLYMERASE ALPHA SUBUNIT, GLYCEROL (3 entities in total) |
| Functional Keywords | transferase, rabies virus, replication, transcription, polymerase, rna-directed rna polymerase, phosphorylation |
| Biological source | Rabies virus CVS-11 |
| Total number of polymer chains | 1 |
| Total formula weight | 13172.94 |
| Authors | Mavrakis, M.,McCarthy, A.A.,Roche, S.,Blondel, D.,Ruigrok, R.W.H. (deposition date: 2004-04-30, release date: 2004-10-15, Last modification date: 2024-05-08) |
| Primary citation | Mavrakis, M.,Mccarthy, A.A.,Roche, S.,Blondel, D.,Ruigrok, R.W.H. Structure and Function of the C-Terminal Domain of the Polymerase Cofactor of Rabies Virus J.Mol.Biol., 343:819-, 2004 Cited by PubMed Abstract: The phosphoprotein (P) of rabies virus binds the viral polymerase to the nucleoprotein (N)-RNA template for transcription and replication. By limited protease digestion we defined a monomeric C-terminal domain of P that can bind to N-RNA. The atomic structure of this domain was determined and previously described mutations that interfere with binding of P to N-RNA could now be interpreted. There appears to be two features involved in this activity situated at opposite surfaces of the molecule: a positively charged patch and a hydrophobic pocket with an exposed tryptophan side-chain. Other previously published work suggests a conformational change in P when it binds to N-RNA, which may imply the repositioning of two helices that would expose a hydrophobic groove for interaction with N. This domain of rabies virus P is structurally unrelated to the N-RNA binding domains of the phosphoproteins of Sendai and measles virus that are members of the same order of viruses, the non-segmented negative strand RNA viruses. The implications of this finding for the evolution of this virus group are discussed. PubMed: 15476803DOI: 10.1016/J.JMB.2004.08.071 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
Download full validation report
